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Validated All-in-One™ qPCR Primer for CASP1(NM_001257118.2) Search again
Product ID:
HQP113493
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ICE, IL1BC, P45
Gene Description:
caspase 1
Target Gene Accession:
NM_001257118.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce 2 subunits, large and small, that dimerize to form the active enzyme. This gene was identified by its ability to proteolytically cleave and activate the inactive precursor of interleukin-1, a cytokine involved in the processes such as inflammation, septic shock, and wound healing. This gene has been shown to induce cell apoptosis and may function in various developmental stages. Studies of a similar gene in mouse suggest a role in the pathogenesis of Huntington disease. Alternative splicing of this gene results in five transcript variants encoding distinct isoforms. [provided by RefSeq].
Gene References into function
- CARD-8 protein, a new CARD family member that regulates caspase-1 activation and apoptosis.
- The PYRIN-CARD protein ASC is an activating adaptor for caspase-1.
- regulation of activation of caspase-1-dependent cytokine processing by PYPAF7
- Interleukin-1F7B (IL-1H4/IL-1F7) is processed by this enzyme
- The caspase-1 level was significantly higher in biochemorefractory melanoma patients compared with responders, suggesting that disrupted apoptosis pathways might be involved in the progressive disease and drug resistance.
- inflammasome comprises caspase-1, caspase-5, Pycard/Asc, and NALP1; a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
- Differential rates of frameshift alterations in four repeat sequences of hereditary nonpolyposis colorectal cancer tumors.These repeats consisted of (A)10 in the TGF beta RII, (G)8 in the BAX, (A)8 in the CASP1, and (CCA)7 in the APP genes.
- activation in immune cells by PYPAF5
- Caspase 1 has a role in T-cell protein tyrosine phosphatase-induced apoptosis in a human tumor cell line.
- Exposure to a cytotoxic concentration of gp120 up-regulates expression of the inducible isoform of cyclooxygenase (COX-2) in neuroblastoma cells and this is blocked by caspase 1 inhibitors
- Caspases responsible for parkin cleavage were identified by several experimental paradigms exploring the anti-Fas induced pathway and tnf-alpha pathway.
- Data show that gingival fibroblasts express interleukin-1 (IL_1) beta converting enzyme mRNA, but low levels of IL-1 beta mRNA, and do not secrete interleukin-18.
- Overexpression of Caspase-1 is a frequent event in pancreatic disorders and neoplasms.
- caspase-1 contributes to inflammation by two distinct pathways: proteolysis of pro-IL-1beta, and RIP2-dependent activation of NF-kappaB and p38 MAPK mediated by the caspase recruitment domain
- resistance of pro-interleukin-18 to processing by caspase 1 in ovarian tumors
- expression of caspase-1 and IL-18 was significantly increased in multiple sclerosis patients
- NF-kappaB- and C/EBPbeta-driven interleukin-1beta gene expression and PAK1-mediated caspase-1 activation play essential roles in interleukin-1beta release from Helicobacter pylori lipopolysaccharide-stimulated macrophages
- epigenetic events such as DNA methylation and histone deacetylation play important roles in the regulation of caspase-1, and loss of caspase-1 expression is associated with poor survival in gastric carcinoma
- data suggest that both pyrin and cryopyrin are capable of assembling independent inflammasome complexes with ASC and procaspase-1, and activating caspase-1 via ASC oligomerization
- VLDL induces IL-1beta mRNA expression, caspase-1 activation, and IL-1beta release from macrophages
- results show that Csp-1 is an upstream positive regulator of Csp-6-mediated cell death in primary human neurons; also results suggest that the activation of Csp-1 must be accompanied by an apoptotic insult to induce Csp-6-mediated cell death
- IL-32 synergizes with nucleotide oligomerization domain (NOD) 1 and NOD2 ligands for IL-1beta and IL-6 production through a caspase 1-dependent mechanism.
- Interleukin-1 Beta gene polymorphism is associated with precancerous lesions in African Americans and Caucasians.
- Increased plasma levels of caspase-1 is associated with cutaneous T-cell lymphoma
- proinflammatory response mediated by statins in activated peripheral blood mononuclear cells is mediated mainly via the activation of caspase-1 and interleukin-18 secretion in the monocytes and to a lesser extent by interleukin-12
- The C-terminal B30.2 domain of pyrin is necessary and sufficient for the interaction with caspase-1 to modulate IL-1beta production.
- Involvement of caspase 1 and its activator Ipaf upstream of mitochondrial events in apoptosis
- IL-32 is a cell-associated proinflammatory cytokine, which is specifically stimulated by mycobacteria through a caspase-1- and IL-18-dependent production of interferon gamma.
- Cop inhibition of cell death, at least to a certain extent, results from its interference with the activation of caspase-1 and caspase-4.
- pannexin-1 is required for processing of caspase-1 and release of mature IL-1beta induced by P2X(7) receptor activation.
- In summary, we showed that HIPPI could interact with the putative promoter sequence of caspase-1 and increased the expression of the downstream gene suggesting that HIPPI could act as transcription regulator.
- Caspase-1 is upregulated in human heart failure and acts as a potent proapoptotic caspase both in isolated human cardiomyocytes and in vivo.
- Caspase-1 plays a role in the regulation of Toll-like receptors-2 and -4 signaling pathways via an effect on MyD88 adapter-like protein.
- Antiapoptotic proteins Bcl-2 and Bcl-X(L) bind and suppress NALP1, reducing caspase-1 activation and interleukin-1beta (IL-1beta) production.
- the activity of caspase-1 is increased in psoriatic skin and IL-18 secretion is regulated by a p38 MAPK/caspase-1-dependent mechanism
- identification of a novel function of HIPPI; it binds to specific upstream sequences of the caspase-1, caspase-8 and caspase-10 genes and alters the expression of the genes
- characterization of caspase-1 substrates identifies the glycolysis pathway as a caspase-1 target and provides new insights into its function during pyroptosis and septic shock.
- Triggering of cytosolic RNA recognition pathway with poly(I:C) transfection or influenza A virus infection resulted in caspase-1- and -3-mediated proteolytic processing of pro-IL-18 and secretion of biologically active IL-18.
- up-regulated in pancreatic sections and in isolated islets from type 2 diabetic patients
- Relative copy numbers for the inflammasome mRNAs for ASC, caspase-1, NALP1, and Pypaf-7 were significantly lower in patients with septic shock compared with critically ill control subjects.
- Study shows that secretion of the leaderless proteins proIL-1alpha, caspase-1, and fibroblast growth factor (FGF)-2 depends on caspase-1 activity.
- Signaling via NADPH oxidase activity is fundamental for the processing of mature IL-1 beta induced in monocytes by ATP receptor P2X7R and caspase-1 activation.
- Data show that Mexico City dogs exhibit frontal white matter upregulation of two important inflammatory genes: COX2 and IL1beta, compared to age-matched control dogs from a low polluted area.
- pyrin is cleaved by caspase-1 at Asp330, a site remote from the B30.2 domain
- X-ray crystal structures of caspase-1 variants suggest the importance of both the salt bridge interaction and the coordination of solvent water molecules near the allosteric binding pocket.
- Frameshift mutation at a mononucleotide repeat in CASP1 is rare in gastric and colorectal carcinomas with microsatellite instability.
- The presence and concentration of caspase-1 in the amniotic fluid varies as a function of gestational age. Women with spontaneous labor at term had a higher median caspase-1 amniotic fluid concentration than women at term without labor.
- a novel mechanism that negatively regulates RIG-I-mediated signaling activity via caspase-1-dependent secretion of RIG-I protein.